SYN1_MOUSE
ID SYN1_MOUSE Reviewed; 706 AA.
AC O88935; Q62279; Q8QZT8;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2005, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Synapsin-1;
DE AltName: Full=Synapsin I;
GN Name=Syn1; Synonyms=Syn-1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM IB).
RC STRAIN=C57BL/6J; TISSUE=Pancreatic islet;
RX PubMed=9890964; DOI=10.1074/jbc.274.4.2053;
RA Matsumoto K., Ebihara K., Yamamoto H., Tabuchi H., Fukunaga K.,
RA Yasunami M., Ohkubo H., Shichiri M., Miyamoto E.;
RT "Cloning from insulinoma cells of synapsin I associated with insulin
RT secretory granules.";
RL J. Biol. Chem. 274:2053-2059(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-125.
RX PubMed=8034599; DOI=10.1016/s0021-9258(17)32338-4;
RA Chin L.S., Li L., Greengard P.;
RT "Neuron-specific expression of the synapsin II gene is directed by a
RT specific core promoter and upstream regulatory elements.";
RL J. Biol. Chem. 269:18507-18513(1994).
RN [4]
RP PROTEIN SEQUENCE OF 86-108; 115-128; 177-186; 257-269; 282-311; 329-336;
RP 414-420; 431-446 AND 566-576, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=C57BL/6J, and OF1; TISSUE=Brain, and Hippocampus;
RA Lubec G., Kang S.U., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP SUBCELLULAR LOCATION, AND INTERACTION WITH PRNP.
RX PubMed=11571277; DOI=10.1074/jbc.m103289200;
RA Spielhaupter C., Schaetzl H.M.;
RT "PrPC directly interacts with proteins involved in signaling pathways.";
RL J. Biol. Chem. 276:44604-44612(2001).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-427, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT THR-87 AND THR-526.
RC TISSUE=Brain;
RX PubMed=16452088; DOI=10.1074/mcp.t500040-mcp200;
RA Vosseller K., Trinidad J.C., Chalkley R.J., Specht C.G., Thalhammer A.,
RA Lynn A.J., Snedecor J.O., Guan S., Medzihradszky K.F., Maltby D.A.,
RA Schoepfer R., Burlingame A.L.;
RT "O-linked N-acetylglucosamine proteomics of postsynaptic density
RT preparations using lectin weak affinity chromatography and mass
RT spectrometry.";
RL Mol. Cell. Proteomics 5:923-934(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-312, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=18034455; DOI=10.1021/pr0701254;
RA Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT "Large-scale identification and evolution indexing of tyrosine
RT phosphorylation sites from murine brain.";
RL J. Proteome Res. 7:311-318(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-9; SER-39; SER-427; SER-432;
RP SER-434; SER-437; SER-438; SER-664; SER-666 AND SER-684, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Brown adipose tissue;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-430; ARG-476; ARG-534; ARG-547;
RP ARG-556; ARG-622 AND ARG-680, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Neuronal phosphoprotein that coats synaptic vesicles, binds
CC to the cytoskeleton, and is believed to function in the regulation of
CC neurotransmitter release. Regulation of neurotransmitter release. The
CC complex formed with NOS1 and CAPON proteins is necessary for specific
CC nitric-oxide functions at a presynaptic level.
CC -!- SUBUNIT: Homodimer. Interacts with CAPON. Forms a ternary complex with
CC NOS1 (By similarity). Isoform Ib interacts with PRNP. {ECO:0000250,
CC ECO:0000269|PubMed:11571277}.
CC -!- SUBCELLULAR LOCATION: Synapse {ECO:0000269|PubMed:11571277}. Golgi
CC apparatus {ECO:0000269|PubMed:11571277}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=Ia;
CC IsoId=O88935-2; Sequence=Displayed;
CC Name=Ib;
CC IsoId=O88935-1; Sequence=VSP_015206, VSP_015207;
CC Name=3;
CC IsoId=O88935-3; Sequence=VSP_015205;
CC -!- DOMAIN: The A region binds phospholipids with a preference for
CC negatively charged species. {ECO:0000250}.
CC -!- PTM: Substrate of at least four different protein kinases. It is
CC probable that phosphorylation plays a role in the regulation of
CC synapsin-1 in the nerve terminal (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation at Ser-9 dissociates synapsins from synaptic
CC vesicles. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the synapsin family. {ECO:0000305}.
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DR EMBL; AF085809; AAD09833.1; -; mRNA.
DR EMBL; BC022954; AAH22954.1; -; mRNA.
DR EMBL; L32025; AAA79963.1; -; Genomic_DNA.
DR CCDS; CCDS53017.1; -. [O88935-2]
DR CCDS; CCDS53018.1; -. [O88935-1]
DR PIR; A53692; A53692.
DR RefSeq; NP_001104250.1; NM_001110780.1. [O88935-1]
DR RefSeq; NP_038708.3; NM_013680.4. [O88935-2]
DR AlphaFoldDB; O88935; -.
DR SMR; O88935; -.
DR BioGRID; 203600; 35.
DR CORUM; O88935; -.
DR IntAct; O88935; 13.
DR MINT; O88935; -.
DR STRING; 10090.ENSMUSP00000111002; -.
DR GlyGen; O88935; 11 sites.
DR iPTMnet; O88935; -.
DR PhosphoSitePlus; O88935; -.
DR SwissPalm; O88935; -.
DR MaxQB; O88935; -.
DR PaxDb; O88935; -.
DR PeptideAtlas; O88935; -.
DR PRIDE; O88935; -.
DR ProteomicsDB; 254840; -. [O88935-2]
DR ProteomicsDB; 254841; -. [O88935-1]
DR ProteomicsDB; 254842; -. [O88935-3]
DR ABCD; O88935; 1 sequenced antibody.
DR Antibodypedia; 403; 1103 antibodies from 45 providers.
DR DNASU; 20964; -.
DR Ensembl; ENSMUST00000081893; ENSMUSP00000080568; ENSMUSG00000037217. [O88935-2]
DR Ensembl; ENSMUST00000115345; ENSMUSP00000111002; ENSMUSG00000037217. [O88935-1]
DR GeneID; 20964; -.
DR KEGG; mmu:20964; -.
DR UCSC; uc009stw.2; mouse. [O88935-2]
DR UCSC; uc009stx.2; mouse. [O88935-1]
DR CTD; 6853; -.
DR MGI; MGI:98460; Syn1.
DR VEuPathDB; HostDB:ENSMUSG00000037217; -.
DR eggNOG; KOG3895; Eukaryota.
DR GeneTree; ENSGT00940000161978; -.
DR HOGENOM; CLU_010582_3_0_1; -.
DR InParanoid; O88935; -.
DR OMA; APMTQGQ; -.
DR OrthoDB; 799740at2759; -.
DR PhylomeDB; O88935; -.
DR TreeFam; TF319919; -.
DR Reactome; R-MMU-181429; Serotonin Neurotransmitter Release Cycle.
DR Reactome; R-MMU-212676; Dopamine Neurotransmitter Release Cycle.
DR BioGRID-ORCS; 20964; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Syn1; mouse.
DR PRO; PR:O88935; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; O88935; protein.
DR Bgee; ENSMUSG00000037217; Expressed in primary visual cortex and 118 other tissues.
DR Genevisible; O88935; MM.
DR GO; GO:0098993; C:anchored component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IDA:MGI.
DR GO; GO:0044297; C:cell body; IDA:MGI.
DR GO; GO:0060203; C:clathrin-sculpted glutamate transport vesicle membrane; TAS:Reactome.
DR GO; GO:0005856; C:cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0030425; C:dendrite; IDA:MGI.
DR GO; GO:0098850; C:extrinsic component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0043229; C:intracellular organelle; ISO:MGI.
DR GO; GO:0043209; C:myelin sheath; HDA:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; IDA:MGI.
DR GO; GO:0098793; C:presynapse; IDA:MGI.
DR GO; GO:0048786; C:presynaptic active zone; IDA:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; ISO:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; IDA:MGI.
DR GO; GO:0000795; C:synaptonemal complex; IDA:MGI.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0048306; F:calcium-dependent protein binding; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; IPI:MGI.
DR GO; GO:0019901; F:protein kinase binding; IPI:ParkinsonsUK-UCL.
DR GO; GO:0048666; P:neuron development; IEA:Ensembl.
DR GO; GO:0007269; P:neurotransmitter secretion; IMP:MGI.
DR GO; GO:0048172; P:regulation of short-term neuronal synaptic plasticity; TAS:ParkinsonsUK-UCL.
DR GO; GO:0098693; P:regulation of synaptic vesicle cycle; IDA:SynGO.
DR GO; GO:0050808; P:synapse organization; ISO:MGI.
DR GO; GO:0097091; P:synaptic vesicle clustering; IMP:SynGO.
DR GO; GO:0099504; P:synaptic vesicle cycle; IMP:SynGO.
DR Gene3D; 3.30.1490.20; -; 1.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR028713; SYN1.
DR InterPro; IPR001359; Synapsin.
DR InterPro; IPR020898; Synapsin_ATP-bd_dom.
DR InterPro; IPR019735; Synapsin_CS.
DR InterPro; IPR019736; Synapsin_P_site.
DR InterPro; IPR020897; Synapsin_pre-ATP-grasp_dom.
DR PANTHER; PTHR10841:SF24; PTHR10841:SF24; 1.
DR Pfam; PF02078; Synapsin; 1.
DR Pfam; PF02750; Synapsin_C; 1.
DR Pfam; PF10581; Synapsin_N; 1.
DR PRINTS; PR01368; SYNAPSIN.
DR SUPFAM; SSF52440; SSF52440; 1.
DR PROSITE; PS00415; SYNAPSIN_1; 1.
DR PROSITE; PS00416; SYNAPSIN_2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; Direct protein sequencing;
KW Glycoprotein; Golgi apparatus; Methylation; Phosphoprotein;
KW Reference proteome; Repeat; Synapse.
FT CHAIN 1..706
FT /note="Synapsin-1"
FT /id="PRO_0000183019"
FT REGION 1..28
FT /note="A"
FT REGION 13..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 29..112
FT /note="B; linker"
FT REGION 113..420
FT /note="C; actin-binding and synaptic-vesicle binding"
FT REGION 419..690
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..657
FT /note="D; Pro-rich linker"
FT REGION 658..706
FT /note="E"
FT COMPBIAS 25..40
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..55
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 419..454
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 455..486
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 511..533
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..555
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..573
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 614..630
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 9
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 39
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 62
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09951"
FT MOD_RES 67
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P09951"
FT MOD_RES 312
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18034455"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 430
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 432
FT /note="Phosphoserine; alternate"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 438
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 476
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 534
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 547
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 551
FT /note="Phosphoserine; by PDPK1"
FT /evidence="ECO:0000250|UniProtKB:P17599"
FT MOD_RES 553
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P17600"
FT MOD_RES 556
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 568
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:P17599"
FT MOD_RES 605
FT /note="Phosphoserine; by CaMK2"
FT /evidence="ECO:0000250|UniProtKB:P17599"
FT MOD_RES 622
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 664
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 666
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 680
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 684
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CARBOHYD 55
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 56
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 87
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 96
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 103
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 261
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 432
FT /note="O-linked (GlcNAc) serine; alternate"
FT /evidence="ECO:0000250"
FT CARBOHYD 518
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT CARBOHYD 526
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000269|PubMed:16452088"
FT CARBOHYD 564
FT /note="O-linked (GlcNAc) threonine"
FT /evidence="ECO:0000250"
FT CARBOHYD 578
FT /note="O-linked (GlcNAc) serine"
FT /evidence="ECO:0000250"
FT VAR_SEQ 573..600
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015205"
FT VAR_SEQ 662..670
FT /note="NKSQSLTNA -> KASPSQAQP (in isoform Ib)"
FT /evidence="ECO:0000303|PubMed:9890964"
FT /id="VSP_015206"
FT VAR_SEQ 671..706
FT /note="Missing (in isoform Ib)"
FT /evidence="ECO:0000303|PubMed:9890964"
FT /id="VSP_015207"
FT CONFLICT 44
FT /note="P -> L (in Ref. 3; AAA79963)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 706 AA; 74097 MW; 04C940E68547372B CRC64;
MNYLRRRLSD SNFMANLPNG YMTDLQRPQP PPPPPSAASP GATPGSATAS AERASTAAPV
ASPAAPSPGS SGGGGFFSSL SNAVKQTTAA AAATFSEQVG GGSGGAGRGG AAARVLLVID
EPHTDWAKYF KGKKIHGEID IKVEQAEFSD LNLVAHANGG FSVDMEVLRN GVKVVRSLKP
DFVLIRQHAF SMARNGDYRS LVIGLQYAGI PSVNSLHSVY NFCDKPWVFA QMVRLHKKLG
TEEFPLIDQT FYPNHKEMLS STTYPVVVKM GHAHSGMGKV KVDNQHDFQD IASVVALTKT
YATAEPFIDA KYDVRVQKIG QNYKAYMRTS VSGNWKTNTG SAMLEQIAMS DRYKLWVDTC
SEIFGGLDIC AVEALHGKDG RDHIIEVVGS SMPLIGDHQD EDKQLIVELV VNKMTQALPR
QPQRDASPGR GSHSQSSSPG ALTLGRQTSQ QPAGPPAQQR PPPQGGPPQP GPGPQRQGPP
LQQRPPPQGQ QHLSGLGPPA GSPLPQRLPS PTAAPQQSAS QATPVTQGQG RQSRPVAGGP
GAPPAARPPA SPSPQRQAGA PQATRQASIS GPAPTKASGA PPGGQQRQGP PQKPPGPAGP
TRQASQAGPG PRTGPPTTQQ PRPSGPGPAG RPAKPQLAQK PSQDVPPPIT AAAGGPPHPQ
LNKSQSLTNA FNLPEPAPPR PSLSQDEVKA ETIRSLRKSF ASLFSD
